Irina Vdovina

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To assess the functional activity of internalized epidermal growth factor (EGF) receptors in A-431 cells we investigated their ability to be both the target and activator of serine and threonine protein kinases. By incubating A-431 cells with EGF at 4 degrees C wr at 37 degrees C, eluting surface-bound EGF with an acid buffer, and immunoprecipitating the(More)
The endocytosis of 125I-EGF was studied in transfectant NIH3T3 cells expressing a normal full-length EGF receptor (HER14) and a mutant receptor lacking 4 major autophosphorylation sites by deletion of 126 amino acids from the carboxyl terminus (CD126). The rates of 125I-EGF internalization and degradation in CD 126 were found to be slightly lower compared(More)
Phosphorylation of the epidermal growth factor (EGF) receptors in endosomes isolated from A431 cells was studied using antiphosphotyrosin antibody (anti-P-Tyr). A431 cells were preincubated with EGF and then washed with acid buffer to remove surface-bound EGF. Endosomes were isolated from such cells by the method of subcellular fractionation on Percoll(More)
Using cultured A431 cells, a comparative analysis was performed of endocytosis stimulated by the epidermal growth factor (EGF) just following the ligand influence (early endocytosis) and after a 3 hour incubation of A431 cells with EGF (delay endocytosis). It is shown that at the early endocytosis the total amount of 125I-EGF, associated with cells, is(More)
A theoretical substantiation and experimental testing of combined adaptation to changing oxygen levels in the enhancement of tolerance to physical loads and pilot study on the protective effects of a novel strategy for adaptation to interval hypoxia-hyperoxia aimed at eliminating the overtraining syndrome in professional athletes, have been carried out.(More)
The ratio of tyrosine-phosphorylated EGF-receptors was estimated for surface and endosomal EGF-receptor complexes on A431 cells. The cells were incubated with 125I-EGF, and then 125I-EGF was covalently bound to the receptor by cross-linking reagent-suberate. Following the cell lysis, the tyrosine-phosphorylated receptors were immunoprecipitated by(More)
The effect of limited proteolysis of myosin subfragment I (S1) on conformational changes in F-actin during the formation of a rigor F-actin-S1 complex was studied, using polarized microfluorimetry. Upon the decoration of thin filaments made up of rhodaminyl-phalloin modified F-actin with subfragment I, the anisotropy of fluorescence increased. Limited(More)
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